ADP Stabilizes the Human Rad51-single stranded DNA Complex and Promotes Its DNA Annealing Activity
Artikel i vetenskaplig tidskrift, 2002

Background: Human Rad51 protein (HsRad51) is a homologue of Escherichia coli RecA protein, and involved in homologous recombination. These eukaryotic and bacterial proteins catalyse strand exchange between two homologous DNA molecules, each forming a complex with single-stranded DNA (ssDNA) and ATP as the initial step. Both proteins hydrolyse ATP; however, the role of ATP hydrolysis appears to vary between the two proteins. Results: Measurements using the fluorescence ssDNA analogue, poly(1,N (6) -etheno-deoxyadenosine), indicate that ATP affects the HsRad51-ssDNA complex, promoting two conformational states: one transient, rather rigid transition state and a final more flexible state. While ADP lowers the affinity of RecA protein to ssDNA, it is found to rather stabilize the HsRad51-ssDNA complex. ADP does not activate the strand exchange by HsRad51 but instead stimulates annealing between complementary ssDNAs. Conclusions: The hydrolysis of ATP promotes a transition of the HsRad51-ssDNA complex from a stiff state to less stiff state. The first state may be important for the strand separation of dsDNA in the initial step of strand exchange, while the second state may be important for annealing in the next step. However, hydrolysis does not dissociate HsRad51 from DNA as a component step of its recycling.

Författare

Hye-Kyung Kim

Institutionen för fysikalisk kemi

Katsumi Morimatsu

Institutionen för fysikalisk kemi

Bengt Nordén

Institutionen för fysikalisk kemi

Malin Ardhammar

Institutionen för fysikalisk kemi

M. Takahashi

Genes to Cells

1356-9597 (ISSN) 1365-2443 (eISSN)

Vol. 7 11 1125-1134

Styrkeområden

Nanovetenskap och nanoteknik

Energi

Livsvetenskaper och teknik

Materialvetenskap

Ämneskategorier

Fysikalisk kemi

Fundament

Grundläggande vetenskaper

DOI

10.1046/j.1365-2443.2002.00588.x

Mer information

Skapat

2017-10-06